AMYP_PIG
ID AMYP_PIG Reviewed; 511 AA.
AC P00690; Q9TUE4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Pancreatic alpha-amylase;
DE Short=PA;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE Flags: Precursor;
GN Name=AMY2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=10082956; DOI=10.1016/s0167-4838(99)00011-4;
RA Darnis S., Juge N., Guo X.-J., Marchis-Mouren G., Puigserver A.,
RA Chaix J.-C.;
RT "Molecular cloning and primary structure analysis of porcine pancreatic
RT alpha-amylase.";
RL Biochim. Biophys. Acta 1430:281-289(1999).
RN [2]
RP PROTEIN SEQUENCE OF 16-511, AND DISULFIDE BONDS.
RX PubMed=3484639; DOI=10.1016/0167-4838(86)90289-x;
RA Pasero L., Mazzei-Pierron Y., Abadie B., Chicheportiche Y.,
RA Marchis-Mouren G.;
RT "Complete amino acid sequence and location of the five disulfide bridges in
RT porcine pancreatic alpha-amylase.";
RL Biochim. Biophys. Acta 869:147-157(1986).
RN [3]
RP DISULFIDE BONDS.
RX PubMed=6188459; DOI=10.1016/0006-291x(83)91021-5;
RA Pasero L., Mazzei Y., Abadie B., Moinier D., Fougereau M.,
RA Marchis-Mouren G.;
RT "Localization of the two free thiol groups in the porcine pancreatic alpha-
RT amylase I sequence.";
RL Biochem. Biophys. Res. Commun. 110:726-732(1983).
RN [4]
RP SUBUNIT, AND INTERACTION WITH THE SEA ANEMONE INHIBITOR MAGNIFICAMIDE.
RX PubMed=31546678; DOI=10.3390/md17100542;
RA Sintsova O., Gladkikh I., Kalinovskii A., Zelepuga E., Monastyrnaya M.,
RA Kim N., Shevchenko L., Peigneur S., Tytgat J., Kozlovskaya E.,
RA Leychenko E.;
RT "Magnificamide, a beta-defensin-like peptide from the mucus of the sea
RT anemone Heteractis magnifica, is a strong inhibitor of mammalian alpha-
RT amylases.";
RL Mar. Drugs 17:0-0(2019).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (5 ANGSTROMS).
RA Payan F., Haser R., Pierrot M., Frey M., Astier J.-P., Abadie B., Duee E.,
RA Buisson G.;
RT "The three-dimensional structure of alpha-amylase from porcine pancreas at
RT 5-A resolution -- the active-site location.";
RL Acta Crystallogr. B 36:416-421(1980).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), COFACTOR, AND DISULFIDE BONDS.
RX PubMed=3502087; DOI=10.1002/j.1460-2075.1987.tb02731.x;
RA Buisson G., Duee E., Haser R., Payan F.;
RT "Three dimensional structure of porcine pancreatic alpha-amylase at 2.9-A
RT resolution. Role of calcium in structure and activity.";
RL EMBO J. 6:3909-3916(1987).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SEQUENCE REVISION.
RX PubMed=8515451; DOI=10.1006/jmbi.1993.1326;
RA Qian M., Haser R., Payan F.;
RT "Structure and molecular model refinement of pig pancreatic alpha-amylase
RT at 2.1-A resolution.";
RL J. Mol. Biol. 231:785-799(1993).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 16-511 IN COMPLEX WITH CALCIUM,
RP DISULFIDE BONDS, AND COFACTOR.
RX PubMed=8193143; DOI=10.1021/bi00186a031;
RA Qian M., Haser R., Buisson G., Duee E., Payan F.;
RT "The active center of a mammalian alpha-amylase. Structure of the complex
RT of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-
RT A resolution.";
RL Biochemistry 33:6284-6294(1994).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 16-511 IN COMPLEX WITH INHIBITOR;
RP CALCIUM AND CHLORIDE, DISULFIDE BONDS, AND COFACTOR.
RX PubMed=7897663; DOI=10.1006/jmbi.1994.0125;
RA Wiegand G., Epp O., Huber R.;
RT "The crystal structure of porcine pancreatic alpha-amylase in complex with
RT the microbial inhibitor Tendamistat.";
RL J. Mol. Biol. 247:99-110(1995).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM;
RP GLUCOSE AND CHLORIDE, DISULFIDE BONDS, AND COFACTOR.
RX PubMed=8757803; DOI=10.1006/jmbi.1996.0410;
RA Machius M., Vertesy L., Huber R., Wiegand G.;
RT "Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-
RT amylase: structure analysis and comparison of their binding
RT characteristics.";
RL J. Mol. Biol. 260:409-421(1996).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM,
RP SEQUENCE REVISION, COFACTOR, AND DISULFIDE BONDS.
RX PubMed=8681972; DOI=10.1111/j.1432-1033.1996.0561z.x;
RA Gilles C., Astier J.-P., Marchis-Mouren G., Cambillau C., Payan F.;
RT "Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex
RT with the carbohydrate inhibitor acarbose.";
RL Eur. J. Biochem. 238:561-569(1996).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 17-511 IN COMPLEX WITH INHIBITOR
RP AND CALCIUM, COFACTOR, AND DISULFIDE BONDS.
RX PubMed=8994970; DOI=10.1016/s0969-2126(96)00151-7;
RA Bompard-Gilles C., Rousseau P., Rouge P., Payan F.;
RT "Substrate mimicry in the active center of a mammalian alpha-amylase:
RT structural analysis of an enzyme-inhibitor complex.";
RL Structure 4:1441-1452(1996).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM
RP AND CHLORIDE, DISULFIDE BONDS, AND COFACTOR.
RX PubMed=9385631; DOI=10.1002/pro.5560061102;
RA Qian M., Spinelli S., Driguez H., Payan F.;
RT "Structure of a pancreatic alpha-amylase bound to a substrate analogue at
RT 2.03-A resolution.";
RL Protein Sci. 6:2285-2296(1997).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) IN COMPLEX WITH CALCIUM; CHLORIDE
RP AND OLIGOSACCHARIDE INHIBITOR, COFACTOR, AND DISULFIDE BOND.
RX PubMed=11412124; DOI=10.1021/bi0102050;
RA Qian M., Nahoum V., Bonicel J., Bischoff H., Henrissat B., Payan F.;
RT "Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-
RT resolution structural analysis of an enzyme-inhibitor complex.";
RL Biochemistry 40:7700-7709(2001).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 16-511 IN COMPLEX WITH CALCIUM
RP AND CHLORIDE, DISULFIDE BONDS, AND COFACTOR.
RX PubMed=11960990; DOI=10.1074/jbc.m202327200;
RA Desmyter A., Spinelli S., Payan F., Lauwereys M., Wyns L., Muyldermans S.,
RA Cambillau C.;
RT "Three camelid VHH domains in complex with porcine pancreatic alpha-
RT amylase. Inhibition and versatility of binding topology.";
RL J. Biol. Chem. 277:23645-23650(2002).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH THE SEA ANEMONE
RP INHIBITOR HELIANTHAMIDE, SUBUNIT, AND INTERACTION WITH THE SEA ANEMONE
RP INHIBITOR HELIANTHAMIDE.
RX PubMed=27066537; DOI=10.1021/acscentsci.5b00399;
RA Tysoe C., Williams L.K., Keyzers R., Nguyen N.T., Tarling C., Wicki J.,
RA Goddard-Borger E.D., Aguda A.H., Perry S., Foster L.J., Andersen R.J.,
RA Brayer G.D., Withers S.G.;
RT "Potent human alpha-amylase inhibition by the beta-defensin-like protein
RT helianthamide.";
RL ACS Cent. Sci. 2:154-161(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000250|UniProtKB:P04746};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990,
CC ECO:0000269|PubMed:3502087, ECO:0000269|PubMed:7897663,
CC ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972,
CC ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970,
CC ECO:0000269|PubMed:9385631};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:11412124,
CC ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:3502087,
CC ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8193143,
CC ECO:0000269|PubMed:8681972, ECO:0000269|PubMed:8757803,
CC ECO:0000269|PubMed:8994970, ECO:0000269|PubMed:9385631};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990,
CC ECO:0000269|PubMed:3502087, ECO:0000269|PubMed:7897663,
CC ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:9385631};
CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000269|PubMed:11412124,
CC ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:3502087,
CC ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8757803,
CC ECO:0000269|PubMed:9385631};
CC -!- SUBUNIT: Binds to the sea anemone inhibitor helianthamide and
CC magnificamide. {ECO:0000269|PubMed:27066537,
CC ECO:0000305|PubMed:31546678}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- MISCELLANEOUS: The two forms of this enzyme, I and II, show very
CC similar activities, molecular masses, and compositions and differ only
CC in their isoelectric points. As no evidence for two variants were in
CC the cDNA library of PubMed:10082956, it is most likely that isoform I
CC (PPAI) and isoform II (PPAII) are two forms of the same protein.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/AA/";
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DR EMBL; AF064742; AAF02828.1; -; mRNA.
DR PIR; A25412; ALPGP.
DR RefSeq; NP_999360.1; NM_214195.1.
DR PDB; 1BVN; X-ray; 2.50 A; P=16-511.
DR PDB; 1DHK; X-ray; 1.85 A; A=17-511.
DR PDB; 1HX0; X-ray; 1.38 A; A=16-511.
DR PDB; 1JFH; X-ray; 2.03 A; A=17-511.
DR PDB; 1KXQ; X-ray; 1.60 A; A/B/C/D=16-511.
DR PDB; 1KXT; X-ray; 2.00 A; A/C/E=16-511.
DR PDB; 1KXV; X-ray; 1.60 A; A/B=16-511.
DR PDB; 1OSE; X-ray; 2.30 A; A=17-511.
DR PDB; 1PIF; X-ray; 2.30 A; A=17-511.
DR PDB; 1PIG; X-ray; 2.20 A; A=17-511.
DR PDB; 1PPI; X-ray; 2.20 A; A=16-511.
DR PDB; 1UA3; X-ray; 2.01 A; A=16-511.
DR PDB; 1VAH; X-ray; 2.40 A; A=16-511.
DR PDB; 1WO2; X-ray; 2.01 A; A=16-511.
DR PDB; 3L2L; X-ray; 2.11 A; A=16-511.
DR PDB; 3L2M; X-ray; 1.97 A; A=16-511.
DR PDB; 4X0N; X-ray; 2.60 A; A=17-511.
DR PDBsum; 1BVN; -.
DR PDBsum; 1DHK; -.
DR PDBsum; 1HX0; -.
DR PDBsum; 1JFH; -.
DR PDBsum; 1KXQ; -.
DR PDBsum; 1KXT; -.
DR PDBsum; 1KXV; -.
DR PDBsum; 1OSE; -.
DR PDBsum; 1PIF; -.
DR PDBsum; 1PIG; -.
DR PDBsum; 1PPI; -.
DR PDBsum; 1UA3; -.
DR PDBsum; 1VAH; -.
DR PDBsum; 1WO2; -.
DR PDBsum; 3L2L; -.
DR PDBsum; 3L2M; -.
DR PDBsum; 4X0N; -.
DR AlphaFoldDB; P00690; -.
DR SMR; P00690; -.
DR MINT; P00690; -.
DR STRING; 9823.ENSSSCP00000007308; -.
DR BindingDB; P00690; -.
DR ChEMBL; CHEMBL5730; -.
DR DrugCentral; P00690; -.
DR Allergome; 970; Sus s Amylase.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; P00690; -.
DR PeptideAtlas; P00690; -.
DR PRIDE; P00690; -.
DR ABCD; P00690; 3 sequenced antibodies.
DR GeneID; 397397; -.
DR KEGG; ssc:397397; -.
DR CTD; 397397; -.
DR eggNOG; KOG2212; Eukaryota.
DR InParanoid; P00690; -.
DR BRENDA; 3.2.1.1; 6170.
DR SABIO-RK; P00690; -.
DR EvolutionaryTrace; P00690; -.
DR PRO; PR:P00690; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0004556; F:alpha-amylase activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0031404; F:chloride ion binding; ISS:UniProtKB.
DR GO; GO:0016052; P:carbohydrate catabolic process; ISS:UniProtKB.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Chloride;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Metal-binding; Pyrrolidone carboxylic acid; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:3484639"
FT CHAIN 16..511
FT /note="Pancreatic alpha-amylase"
FT /id="PRO_0000001399"
FT ACT_SITE 212
FT /note="Nucleophile"
FT ACT_SITE 248
FT /note="Proton donor"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11412124,
FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663,
FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972,
FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970,
FT ECO:0000269|PubMed:9385631"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11412124,
FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663,
FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972,
FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970,
FT ECO:0000269|PubMed:9385631"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11412124,
FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663,
FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972,
FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970,
FT ECO:0000269|PubMed:9385631"
FT BINDING 210
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:11412124,
FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663,
FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:9385631"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11412124,
FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663,
FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972,
FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970,
FT ECO:0000269|PubMed:9385631"
FT BINDING 313
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000305"
FT BINDING 352
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:11412124,
FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663,
FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:9385631"
FT SITE 315
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT MOD_RES 16
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 43..101
FT /evidence="ECO:0000269|PubMed:11412124,
FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663,
FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972,
FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970,
FT ECO:0000269|PubMed:9385631, ECO:0000305|PubMed:3502087"
FT DISULFID 85..130
FT /evidence="ECO:0000269|PubMed:11412124,
FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663,
FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972,
FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970,
FT ECO:0000269|PubMed:9385631, ECO:0000305|PubMed:3502087"
FT DISULFID 156..175
FT /evidence="ECO:0000269|PubMed:11412124,
FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663,
FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972,
FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970,
FT ECO:0000269|PubMed:9385631, ECO:0000305|PubMed:3502087"
FT DISULFID 393..399
FT /evidence="ECO:0000269|PubMed:11412124,
FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663,
FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972,
FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970,
FT ECO:0000269|PubMed:9385631, ECO:0000305|PubMed:3502087"
FT DISULFID 465..477
FT /evidence="ECO:0000269|PubMed:11412124,
FT ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663,
FT ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972,
FT ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970,
FT ECO:0000269|PubMed:9385631, ECO:0000305|PubMed:3502087"
FT CONFLICT 138
FT /note="N -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="A -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:1HX0"
FT TURN 46..51
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:1HX0"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1PIF"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1KXQ"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1HX0"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1HX0"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1KXV"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 188..204
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:1HX0"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:1HX0"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:1KXQ"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 333..345
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:3L2M"
FT TURN 369..372
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 404..415
FT /evidence="ECO:0007829|PDB:1HX0"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 421..426
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 428..436
FT /evidence="ECO:0007829|PDB:1HX0"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 440..445
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 451..456
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:1HX0"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 476..479
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 488..494
FT /evidence="ECO:0007829|PDB:1HX0"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:1KXQ"
FT STRAND 502..506
FT /evidence="ECO:0007829|PDB:1HX0"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:1HX0"
SQ SEQUENCE 511 AA; 57086 MW; 117489E020807378 CRC64;
MKLFLLLSAF GFCWAQYAPQ TQSGRTSIVH LFEWRWVDIA LECERYLGPK GFGGVQVSPP
NENIVVTNPS RPWWERYQPV SYKLCTRSGN ENEFRDMVTR CNNVGVRIYV DAVINHMCGS
GAAAGTGTTC GSYCNPGNRE FPAVPYSAWD FNDGKCKTAS GGIESYNDPY QVRDCQLVGL
LDLALEKDYV RSMIADYLNK LIDIGVAGFR IDASKHMWPG DIKAVLDKLH NLNTNWFPAG
SRPFIFQEVI DLGGEAIQSS EYFGNGRVTE FKYGAKLGTV VRKWSGEKMS YLKNWGEGWG
FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKVAV GFMLAHPYGF TRVMSSYRWA
RNFVNGQDVN DWIGPPNNNG VIKEVTINAD TTCGNDWVCE HRWRQIRNMV WFRNVVDGQP
FANWWANGSN QVAFGRGNRG FIVFNNDDWQ LSSTLQTGLP GGTYCDVISG DKVGNSCTGI
KVYVSSDGTA QFSISNSAED PFIAIHAESK L
